INSTITUTO DE BIOTECNOLOGIA Y BIOLOGIA MOLECULAR
Unidad Ejecutora - UE
congresos y reuniones científicas
Analysis of a Bordetella bronchiseptica cyclic-di-GMP-binding protein reveals a role in motility and virulence.
SISTI, FEDERICO; FERNANDEZ, JULIETA
Potrero de los Funes, San Luis
Congreso; XLVII Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2011
Bis(3′,5′)-cyclic diguanylic acid (c-di-GMP) is a cyclic dinucleotide that has recently been recognized as an important intracellular signaling molecule in diverse bacteria. The intracellular concentration of c-di-GMP is regulated by the opposing activities of diguanylate cyclase (DGC) and phosphodiesterase (PDE) enzymes. PilZ domain-containing proteins have been demonstrated to bind c-di-GMP and to serve as important downstream effector proteins and have been implicated in bacterial motility and pathogenesis of several pathogens.Bordetella bronchiseptica is a pathogenic bacterium that causes respiratory infections in a wide variety of host. We determined that the only PilZ containing domain protein in B. bronchiseptica (BB1561) is able to specifically bind c-di GMP. In a previous work we determined that high c-di-GMP enhances biofilm formation and decreases motility in B. bronchiseptica. We constructed a deletion mutant in BB1561 and determined that biofilm formation was enhanced and motility was reduced compared to parental strain. Furthermore, experimental mice colonization was reduced in BB1561 mutant compared to parental strain.